Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues tyr946-Thr-Val and requires phosphorylation of Thr947
Anja T. Fuglsang,Sabina Visconti,Katrine Drumm,Thomas Jahn,Allan Stensballe,Benedetta Mattei,Ole N. Jensen,Patrizia Aducci,Michael G. Palmgren +8 more
TLDR
The extreme end of AHA2 contains an unusual high-affinity binding site for 14-3-3 protein, which is in practice irreversible in the presence of fusicoccin.About:
This article is published in Journal of Biological Chemistry.The article was published on 1999-12-17 and is currently open access. It has received 311 citations till now. The article focuses on the topics: Vesicle-associated membrane protein 8 & Binding site.read more
Citations
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PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake.
TL;DR: The elucidation of the three-dimensional structure of a related Ca2+ pump has implications for understanding of structure-function relationships for the plant plasma membrane H+-ATPase.
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How do 14-3-3 proteins work? – Gatekeeper phosphorylation and the molecular anvil hypothesis
TL;DR: A speculative model where binding of 14‐3‐3 to multiple sites on some ligands results in global ligand conformational changes that mediate their biological effects is presented and may prove to be a bona fide phosphodependent signaling chaperone.
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Large-scale Analysis of in Vivo Phosphorylated Membrane Proteins by Immobilized Metal Ion Affinity Chromatography and Mass Spectrometry
TL;DR: A scheme for two-dimensional peptide separation using strong anion exchange chromatography prior to IMAC that both decreases the complexity of IMAC-purified phosphopeptides and yields a far greater coverage of monophosphorylated peptides is presented.
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Biology, structure and mechanism of P-type ATPases
TL;DR: Recent X-ray structures and homology models of P-type pumps now provide a basis for understanding the molecular mechanism of ATP-driven ion transport.
Journal ArticleDOI
P-Type ATPases
Michael G. Palmgren,Poul Nissen +1 more
TL;DR: The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines.
References
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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
TL;DR: Silver staining allows a substantial shortening of sample preparation time and may, therefore, be preferable over Coomassie staining, and this work removes a major obstacle to the low-level sequence analysis of proteins separated on polyacrylamide gels.
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Fluorescent indicators for Ca2+based on green fluorescent proteins and calmodulin
Atsushi Miyawaki,Juan Llopis,Roger Heim,J. Michael McCaffery,Joseph A. Adams,Mitsuhiko Ikura,Mitsuhiko Ikura,Roger Y. Tsien +7 more
TL;DR: New fluorescent indicators for Ca2+ that are genetically encoded without cofactors and are targetable to specific intracellular locations are constructed and dubbed ‘cameleons’.
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Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
Matthias Wilm,Andrej Shevchenko,Tony Houthaeve,Stephen Breit,Lothar Schweigerer,Lothar Schweigerer,Theodore Fotsis,Matthias Mann +7 more
TL;DR: A simple and robust technique for the sequencing of proteins isolated by polyacrylamide gel electro-phoresis, using nano-electrospray3,4 tandem mass spectrometry5,6 and multiple-sequence stretches of up to 16 amino acids are obtained.
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The structural basis for 14-3-3:phosphopeptide binding specificity.
Michael B. Yaffe,Katrin Rittinger,Stefano Volinia,Paul R. Caron,Alastair Aitken,Henrik Leffers,Steven J. Gamblin,Stephen J. Smerdon,Lewis C. Cantley,Lewis C. Cantley +9 more
TL;DR: It is shown that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl.
Journal ArticleDOI
The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.
Tim Durfee,Kathleen Becherer,Phang Lang Chen,Shiou-Hwei Yeh,Yanzhu Yang,April E. Kilburn,Wen-Hwa Lee,Stephen J. Elledge +7 more
TL;DR: An improved version of the yeast two-hybrid system is developed and used to isolate human cDNAs encoding proteins able to bind p110RB to demonstrate that PP-1 alpha isoforms preferentially bind the hypophosphorylated form of p110 RB.